First name,Last name,Preferred title,Overview,Position,Department,Individual
Dorothy,Shippen,Professor,"We are taking biochemical, molecular genetic and cytological approaches to study the structure, function and maintenance of telomeres. Telomeres are higher order nucleoprotein complexes that cap the ends of eukaryotic chromosomes and play essential roles in conferring genome stability and cell proliferation capacity. The protective cap of the telomere is comprised of specific telomere binding proteins that regulate the length of telomeric DNA tract and allow the cell distinguish the chromosome terminus from a double-strand break. Telomeric DNA is synthesized by the action of telomerase, an unusual reverse transcriptase that replenishes telomeric DNA lost as a consequence of replication by conventional DNA polymerases. We have developed the genetically tractable flowering plant Arabidopsis thaliana as a model system for studying telomeres in higher eukaryotes. With its sequenced genome, abundant genetic and transgenic tools, and extraordinarily high tolerance to genome instability, Arabidopsis has proven to be an excellent model for investigating fundamental processes in telomere biology. Current studies focus on defining the function and molecular evolution of telomere capping proteins and components of the telomerase ribonucleoprotein complex.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n07e86cac
Libo,Shan,Professor,"Earth is the planet of the plants. Being autotrophic, sessile, and long-living entities, plants have evolved fascinating strategies to cope with various environmental stresses. Our research is driven by the desire to understand the fundamental principles underlying plant disease resistance, and pathogen virulence, and to improve crop resilience to pathogen infections. We are probing the biochemical and genetic basis of plant signal transduction pathways from cell surface receptors sensing the presence of pathogens to signaling cascades and target genes and proteins that are central to launch effective immune responses in the context of balanced growth and development. We deploy cutting-edge molecular and biochemical technologies coupled with powerful genetic tractability of plants for discovering regulatory networks of living organisms fending off infections. In addition to the acquisition of foundational principles in biology, we further translate knowledge and platforms into the areas for the improvement of crop stress adaptation.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n2c655431
Pingwei,Li,Professor,"The research in my lab focuses on elucidating the structural basis of innate immune responses towards microbial nucleic acids. The cGAS/STING pathway plays a central role in innate immunity toward bacterial and viral DNA. cGAS is activated by dsDNA and catalyzes the synthesis of a cyclic dinucleotide cGAMP, which binds to the adaptor STING that mediates the recruitment and activation of protein kinase TBK1 and transcription factor IRF-3. Activated IRF-3 translocates to the nucleus and induces the expression of type I interferons (IFN), an important family of antiviral cytokine. To elucidate the mechanism of cGAS activation, we determined the structures of cGAS in isolation and in complex with DNA. The cGAS/DNA complex structure reveals that cGAS interacts with DNA through two binding sites. Enzyme assays and IFN-? reporter assays of cGAS mutants demonstrate that interactions at both DNA binding sites are essential for cGAS activation. To investigate how cGAMP activates STING, we determined the structures of STING in isolation and in complex with cGAMP. These structures reveal that STING forms a V-shaped dimer and binds cGAMP at the dimer interface. We have also determined the structures of TBK1 in complex with two inhibitors, which show that TBK1 exhibits an I?B kinase fold with distinct domain arrangement. To elucidate the mechanism of IRF-3 recruitment by STING, we determined the structure of a phosphorylated STING peptide bound to IRF-3. To understand how phosphorylation activates IRF-3, we solved the structure of an IRF-3 phosphomimetic mutant bound to CBP, which reveals how phosphorylation induces the dimerization and activation of IRF-3.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n31ebad17
Ping,He,Professor,"Our laboratory is interested in elucidating novel plant immune signaling pathways as well as studying the myriad actions of pathogen virulence factors that intercept host immune responses. In order to provide a complete view of host-microbe interactions, we are using cellular, functional genomic, genetic, biochemical and bioinformatic approaches. In addition, plant immunity is inextricably linked with plant development and environmental stresses. We are also interested in understanding the signaling crosstalk that orchestrates plant responses to different extrinsic and intrinsic signals. Ultimately, knowledge gained from studying model plants, such as Arabidopsis, will be applied to improve crop plants for resistance against different biotic and abiotic stresses.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n330081c7
Jennifer,Herman,Associate Professor,"The study of how bacteria organize important cellular processes and determining the functional/physiological implications of this organization for the cell is one of the most exciting areas of research in microbiology. In the Herman lab, we utilize the model organism Bacillus subtilis, a bacterium with superb molecular, genetic and cell biological tools, that that can also differentiate into a resting cell type called a spore. Our research goal is to elucidate how bacteria coordinate key biological processes, with their cellular architecture using molecular, biochemical, and cell biological techniques.",Associate Professor||Associate Professor,Texas A&M AgriLife Research||Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n359e91fd
Thomas,Meek,Professor,"Marketed drugs have been developed for representatives of all six classes of enzymes, and comprise essential therapies for the treatment of cancers, HIV/AIDS, hypercholesterolemia, and bacterial infections. The availability of known point mutations that are causative of human cancers , as well as the full genomic descriptions of many pathogens, such as parasitic protozoa and infectious bacteria, provides an emerging means to identify new or known enzymes that would constitute potential drug targets. Likewise, the availability of crystal structures of many of these enzymes or their analogues, provides a means to rationally design new inhibitors of enzyme drug targets via the use of molecular modelling and a full understanding of the chemical mechanism of the target enzymes, as an important adjuvant to inhibitor discovery via high-throughput screening.
Our laboratory will initially focus on the detailed study of the mechanisms of cysteine proteases such as cathepsin C, the isocitrate lyase of Mycobacterium tuberculosis, and human ATP-citrate lyase, by the use of pre-steady-state and steady-state kinetics, as well as by use of existing crystal structures of these enzymes, to inform the design of both covalent and other mechanism-based modes for the inactivation of these enzymes. We will design and synthesize candidate inhibitors, and test them against these and other enzyme targets, and determine their suitability as potential drug candidates.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n41081941
Geoffrey,Kapler,Professor and Chair,"Dr. Kapler's broad research interests are concerned with the replication and transmission of eukaryotic chromosomes. The failure to completely replicate the genome during S phase or partially re-replicate chromosomes leads to genome instability- a hallmark of cancer cells. The central questions investigated in the laboratory are concerned with how replication initiation sites are established in chromosomes and how they are regulated during conventional (G1/S/G2/M) and alternative cell cycles, including endoreplication (gap-S-gap-S...) and locus-specific gene amplification. The current focus of the lab is to use high throughput (nascent strand) DNA sequencing to generate a comprehensive map of replication initiation sites under different physiological conditions.",Professor and Chair||Professor,Cell Biology and Genetics||Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n4128afa1
Paul,Straight,Associate Professor,"Our goal is to understand how microorganisms interact in complex communities. Specifically, we study how small molecules produced in a microbial community affect the growth, development and metabolic output of the organisms. We use a combination of microbiology, genetic, genomic, and biochemical approaches to dissect complex interspecies interactions. Currently, our research focuses on the interactions of the soil bacteria Bacillus subtilis and members of the genus Streptomyces, known for their prolific production of bioactive small molecules and development of aerial structures and spores.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n5540637b
Joshua,Wand,Professor and Department Head,"We are broadly interested in how the biophysical properties of proteins are manifested in their biological function. We are particularly engaged in trying to reveal the nature of internal protein motion and how this influences functions ranging from molecular recognition to allostery and catalysis. These basic ideas are being employed in a range of studies including protein engineering to optimize protein drugs, reverse micelle encapsulation to aid fragment-based drug discovery, understanding the regulation of Parkin, which is involved in mitophagy and early onset Parkinson's Disease, and the enzyme AKR1C3, which is central to resistant forms of prostate cancer.",Professor and Department Head,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n6caf5ddd
Sumana,Datta,Assistant Provost,"We are currently investigating how organismal level cues regulate the onset of stem cell division during development. Our primary system is the neuroblasts in the brain of the fruit fly, Drosophila melanogaster. The trol gene of Drosophila encodes the fly homolog of the mammalian heparan sulfate glycoprotein, Perlecan. Perlecan is found in mice, humans, and C. elegans, and is widely known as a co-receptor for the growth factor FGF. We have shown that Trol, the Drosophila Perlecan homolog, is required for signaling by FGF. Furthermore, we have demonstrated that Trol is also a likely candidate for the Hedgehog co-receptor. Hedgehogs are peptide growth factors which are conserved in mammals and require heparan sulfate glycoproteins for their movement and long-range signaling; however, until now the identity of the protein core was unknown. Our studies demonstrate genetic interactions between trol and hedgehog or patched mutations (patched is the Hedgehog receptor). Further studies reveal that both FGF and Hedgehog signaling activate stem cell division. Current projects involve determining how Trol stimulates FGF and Hedgehog signaling through genetic, molecular, and biochemical analyses.",Assistant Provost,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n8ce436a7
David,Threadgill,Professor,"Our laboratory uses the mouse as an experimental genetic model to investigate factors that contribute to inter-individual differences in health and disease. Ourcurrent research activities include the identification and functional characterization of alleles contributing to cancer susceptibility, the function of theErbbgenefamily in development and disease, and the role of genetic variation in response to environmental stimuli. To support these investigations, we also aredeveloping new genetic tools to support mammalian systems genetic approaches to phenotypes with complex genetic and environmental etiologies.",Director||Professor||Professor||Professor,Cell Biology and Genetics||Institute of Genome Sciences and Society||Biochemistry and Biophysics||Nutrition,https://scholars.library.tamu.edu/vivo/display/n8ee0b54f
James,Sacchettini,Professor,"My lab uses X-ray crystallography to better understand the relationship between proteins and ligands. Tiny differences in the structure of a molecule can radically change the interaction between a protein and ligand and we are only begining to understand how many factors play a role in this interaction. By manipulating the individual components of a compound it is possible to create a chemical that binds to the protein better than the natural substrate, and prevent the natural reaction from occurring. This is the basis for rational drug design. Our efforts have lead us to collaborations with other labs and scientists in many disciplines as our approach to directed compound design has applications not only in basic research but also in pesticide development, health research and clinical research.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n90385563
Vytas,Bankaitis,Professor,"My laboratory is interested in the regulatory interfaces between novel lipid-mediated signal transduction pathways and important cellular functions. The focus of our work is the phosphatidylinositol/ phosphatidylcholine transfer proteins (PITPs), a ubiquitous but enigmatic class of proteins. Ongoing projects in the laboratory derive from a multidisciplinary approach that encompasses biochemical characterization of novel members of the metazoan PITP family, and the application of genetic, molecular and biophysical approaches to detailed structural and functional analyses of PITPs.",E.L. Wehner-Welch Foundation Chair||Professor||Professor,Cell Biology and Genetics||Biochemistry and Biophysics||Chemistry,https://scholars.library.tamu.edu/vivo/display/ncff8dc21
Hays,Rye,Associate Professor,"A fundamental principle of biology is the use of chemical energy in the form of ATP to assemble, disassemble and alter macromolecular structure. Specialized control proteins known as molecular chaperones are often responsible for this activity and have been recognized in recent years to be essential for regulating many aspects of cellular biology. Using a variety of biophysical and biochemical techniques, the Rye lab focuses on three fundamental cellular processes that require molecular chaperones: (1) protein folding (2) protein disaggregation and (3) vesicle trafficking. In each of these cases, large quantities ATP are burned, resulting in molecular organization in the case of protein folding, and molecular disassembly and remodeling in the case of protein disaggregation and vesicle trafficking. We are interested in understanding the detailed biophysical mechanisms that underpin these events. Why are these processes so energetically expensive? Are there any similarities in how the energy is used between these very different molecular processes? Are there general principles of energy transduction in biology that can be gleaned by comparing these examples with other molecular machines, such as cytoskeletal motors? Understanding how molecular chaperones control protein and membrane organization will provide key insights into not only basic cell biology, but will also illuminate aspects of many diseases that spring from aberrant protein and membrane dynamics.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/ne7fb85e1
Ryland,Young,Professor,"Most bacterial viruses (phages) cause lysis of their host cell to release the progeny virions. Large phages elaborate an enzyme (""endolysin"") to degrade the cell wall and also a small membrane protein (""holin""). The holin accumulates in the membrane and then, at a precisely scheduled time, suddenly forms a hole to allow release of endolysin through the cytoplasmic membrane to gain access to the wall. We use molecular genetics and biochemistry to study how this small protein is able to act as a molecular ""clock"" and punch holes in membranes. Small phages make single proteins which cause host lysis in a different way. This strategy is to target the host cell wall synthesis machinery; that is, the virus makes a ""protein antibiotic"" that causes lysis in the same way as antibiotics like penicillin by inhibiting an enzyme in the multi-step pathway of murein biosynthesis. Thus, when the infected cell tries to divide, it blows up, or lyses, because it can't make the new cell wall between the daughter cells. Remarkably, each of three different, small phages blocks a different step in the pathway. These small lysis proteins are models for a completely new class of antibacterial antibiotics. Also, the E. coli SlyD protein is required for this mode of lysis in one case. SlyD is a member of an ubiquitous family of proteins related to human ""immunophilins,"" the targets of immune-suppression drugs. We study SlyD to learn about the role of this class of proteins in biology.",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/nea775348
John,Mullet,Professor,"Functional genomics, bioinformatics, and DNA chip technology are fundamentally changing research on biological systems. Knowledge of complete genome sequences and high resolution genome technology provide an extraordinary opportunity to understand complex biological processes and to relate detailed understanding of protein structure and biochemical mechanism to the function of whole organisms and biological systems in nature.
Our research team is helping to build genome maps and DNA diagnostic microarrays/chips for analysis of global gene expression and biodiversity. This new technology is being used to explore the molecular basis of several fundamental plant responses: (1) light responsive genetic systems that help protect plants from damage by high intensity UV/blue light; (2) genetic systems that allow plants to adapt to the environment; (3) genes and signal transduction pathways that help protect plants from insects and disease; and (4) genes that regulate plant development (flowering time, fertility restoration, chloroplast development/number).",Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/nf1c81fcb